[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain cortex; Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.; "Isolation and characterization of cDNA for macaque neurological disease genes."; Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate (By similarity).
SUBUNIT: Heterotetramer of alpha and beta chains (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
MISCELLANEOUS: Bound potassium ions stabilize the protein structure (By similarity).
SIMILARITY: Belongs to the BCKDHA family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB083305; BAC20584.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P12694; 1OLX. [HSSP ENTRY / PDB]

SMR

Q8HXY4; 51-445.

ModBase

Q8HXY4.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003863;	Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity (inferred from electronic annotation from EC).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001017; DHase_E1.
Graphical view of domain structure.

Pfam

PF00676; E1_dh; 1.
Pfam graphical view of domain structure.

Phylogenomic databases

HOVERGEN

Q8HXY4; -.

Other

ProtoNet

Q8HXY4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein; Potassium; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 45`	`45`	`Mitochondrion (By similarity).`
`CHAIN`	`46 445`	`400`	`2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial.`	`PRO_0000020466`
`REGION`	`157 159`	`3`	`Thiamine pyrophosphate binding (By similarity).`
`METAL`	`206 206`		`Potassium (By similarity).`
`METAL`	`211 211`		`Potassium (By similarity).`
`METAL`	`212 212`		`Potassium (By similarity).`
`MOD_RES`	`337 337`		`Phosphoserine (By similarity).`
`MOD_RES`	`345 345`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`347 347`		`Phosphoserine (By similarity).`

Sequence information

Length: 445 AA [This is the length of the unprocessed precursor]

Molecular weight: 50538 Da [This is the MW of the unprocessed precursor]

CRC64: AF645FF711238CA4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVAIAAARV WRPNRGLSQA ALLLLWRPGA RGLARSHPHR QQQQFSSLDD KPQFPGASAE 

        70         80         90        100        110        120 
FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE KVLKLYKSMT LLNTMDRILY 

       130        140        150        160        170        180 
ESQRQGRISF YMTNYGEEGT HVGSAAALDN TDLVFGQYRE AGVLMYRDYP LELFMAQCYG 

       190        200        210        220        230        240 
NISDLGKGRQ MPVHYGCKER HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA 

       250        260        270        280        290        300 
ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG YGIMSIRVDG 

       310        320        330        340        350        360 
NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE VNYWDKQDHP 

       370        380        390        400        410        420 
ISRLRHYLLS QGWWDEEQEK AWRKQSRKKV MKAFEQAERK PKPNPNLLFS DVYQEMPAQL 

       430        440 
RKQQESLARH LQTYGEHYPL EHFDK

Q8HXY4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools